BMRB Entry 18118

Name: NMR structure of the protein BC040485 from Homo sapiens
Published: 2012-01-25

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PDB ID: 2lmi
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR18118
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Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

NMR structure of the protein BC040485 from Homo sapiens

Deposition date:

2011-12-01

Original release date:

2012-01-25

Authors:

Dutta, Samit; Serrano, Pedro; Geralt, Michael; Wuthrich, Kurt; JCSG, JCSG

Citation:

Citation: Dutta, Samit; Serrano, Pedro; Geralt, Michael; Wuthrich, Kurt. "NMR structure of the human RNA binding protein BC040485" .

Assembly members:

Assembly members:
entity, polymer, 107 residues, 12443.094 Da.

Natural source:

Natural source: Common Name: Human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pSpeedET

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity: GSKLEEEVDDVFLIRAQGLP WSCTMEDVLNFFSDCRIRNG ENGIHFLLNRDGKRRGDALI EMESEQDVQKALEKHRMYMG QRYVEVYEINNEDVDALMKS LQVKSSP

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	340
15N chemical shifts	113
1H chemical shifts	698

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	BC040485	1

Entities:

Entity 1, BC040485 107 residues - 12443.094 Da.

1

GLY

SER

LYS

LEU

GLU

VAL

ASP

2

VAL

PHE

LEU

ILE

ARG

ALA

GLN

GLY

LEU

PRO

3

TRP

SER

CYS

THR

MET

GLU

ASP

VAL

LEU

ASN

4

PHE

SER

ASP

CYS

ARG

ILE

ARG

ASN

GLY

5

GLU

ASN

GLY

ILE

HIS

PHE

LEU

ASN

ARG

6

ASP

GLY

LYS

ARG

GLY

ASP

ALA

LEU

ILE

7

GLU

MET

GLU

SER

GLU

GLN

ASP

VAL

GLN

LYS

8

ALA

LEU

GLU

LYS

HIS

ARG

MET

TYR

MET

GLY

9

GLN

ARG

TYR

VAL

GLU

VAL

TYR

GLU

ILE

ASN

10

ASN

GLU

ASP

VAL

ASP

ALA

LEU

MET

LYS

SER

11

LEU

GLN

VAL

LYS

SER

PRO

Samples:

sample_1: entity, [U-98% 13C; U-98% 15N], 1.2 mM; sodium phosphate 20 mM; sodium azide 5 mM; sodium chloride 50 mM; H2O 95%; D2O 5%

sample_conditions_1: ionic strength: 0.080 M; pH: 6.0; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
4D HACANH	sample_1	isotropic	sample_conditions_1
5D HACACONH	sample_1	isotropic	sample_conditions_1
5D CBCACONH	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aliphatic	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aromatic	sample_1	isotropic	sample_conditions_1

Software:

CYANA, G ntert P. - structure solution

TOPSPIN, Bruker Biospin - collection, processing

CARA, Keller and Wuthrich - chemical shift assignment, data analysis

OPAL, Luginbuhl, Guntert, Billeter and Wuthrich - refinement

NMR spectrometers:

Bruker Avance 600 MHz
Bruker Avance 800 MHz